标签： Cosmo Bio LTD

Application: IP, IF, WB

Clonality: Monoclonal

Host: Mouse

Purification: Ammonium Sulfate

Reactivity: Human, Hamster, Chicken

DDB1 was originally identified as a large subunit of damaged DNA-binding protein (DDB), which plays a role in DNA repair. DDB1 also functions as an adaptor molecule of Cul4/DDB1 ubiquitin E3 ligase and participates in various cellular processes.

References:
1) Wakasugi M, Matsuura K, Nagasawa A, Fu D, Shimizu H, Yamamoto K, Takeda S, Matsunaga T. (2007) DDB1 gene disruption causes a severe growth defect and apoptosis in chicken DT40 cells. Biochem Biophys Res Commun. 364(4):771-7. PMID: 17976535.

Application: FC

Clonality: Monoclonal

Host: Rat

Purification: Ig-PG

Reactivity: Zebrafish, Goldfish, Carp

The two major subsets of T lymphocytes, helper and cytotoxic T cells, are defined by expression of CD4 and CD8 glycoproteins, respectively. T cells expressing the CD4 surface antigen facilitate B-cell maturation and production of antibodies by B-cells and are thus termed “helper” T cells. CD4+ helper T cells recognize exogenously derived peptides in the context of MHC class II molecule expressed on antigen presenting cells. One (D1) of four Ig-like extracellular domains of CD4 primarily interacts with the α2 and β2 domains of the MHC class II heterodimer. This antibody, raised against antigens from Ginbuna carp, permits flow cytometric and immunofluorescence analysis of CD4 helper T cells from zebrafish, goldfish and the cyprinid fish carp.

Source: Dr. Teruyuki Nakanishi, Department of Veterinary Medicine, Faculty of Materials Science and Technology, University of Japan

References:
1) Toda H., et al. Conservation of characteristics and functions of CD4 positive lymphocytes in a teleost fish. Dev Comp Immunol. (2011) 35 (6), 650-660.
2) Shibasaki Y., et al. Kinetics of CD4 + and CD8α + T-cell subsets in Graft-Versus-Host Reaction (GVHR) in Gimbuna crucian carp Carassius auratus langsdorfii.

Application: IHC, WB

Clonality: Polyclonal

Host: Rabbit

Purification: Purified – Affinity

Reactivity: Mouse

Septin 5 (Sept5) is a member of the Septin GTPase family and is thought to be involved in exocytosis through interactions with syntaxin 1 in postmitotic neurons. In rats, Sept5 is alternatively spliced to produce a short (Sept5_v2) and long (Sept5_v1) isoform. We recently identified Sept5 in rat brain as a substrate for Cdk5/p35, which phosphorylates Ser17 of Sept5_v1. To date, however, only the short Sept5_v2 isoform has been reported in the mouse. To determine the general expression of the Sept5_v1 isoform in mammals, we isolated Sept5_v1 cDNA by PCR using mouse brain total RNA. Mouse Sept5_v1 cDNA showed a high degree of nucleotide and amino acid sequence homology to the corresponding isoform of rat and human Sept5. Both isoforms were expressed mainly in brain and testis at the mRNA level, but expression was restricted to brain at the protein level. Whereas Sept5_v1 mRNA was highly expressed in the cortex and hippocampus, Sept5_v2 mRNA was expressed at the similar extent across in various brain regions. The protein ratio of Sept5_v1 to Sept5_v2 was high in the hippocampus, roughly equivalent in the cortex and low in the cerebellum and medulla. Sept5_v2 expression increased gradually from E17 to P30, but expression of Sept5_v1 was delayed until P10. The two isoforms were distinguished by their pattern of N-terminal phosphorylation. Thus, these different expression and phosphorylation patterns suggest isoform-specific functions for Sept5 and that a phosphorylation-specific antibody will be useful to study this idea. [from: Asada A1, Takahashi J, Taniguchi M, Yamamoto H, Kimura T, Saito T, Hisanaga S. Neuronal expression of two isoforms of mouse Septin 5. J Neurosci Res. 2010 May 1;88(6):1309-16. doi: 10.1002/jnr.22294.]

Application: IHC, WB

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Human, Mouse

Neurodegenerative diseases such as Alzheimer’s disease and Parkinson’s disease have been increasing rapidly and have become a serious social problem. In recent years, new causative genes have been discovered for amyotrophic lateral sclerosis (ALS) and other intractable neurological diseases opening new avenues for research on pathogenesis. It has been suggested that aggregation and accumulation of specific proteins cause neurotoxicity and the formation of lesions, but the onset and progression mechanisms are still unclear. Neuropathological diagnostic and experimental model biomarkers are needed for drug construction, drug discovery, and therapeutic development.

Alpha-Synuclein, a 140-amino acid protein abundantly expressed in presynaptic terminals, is a component of intraneuronal or glial inclusions observed in cases of Parkinson’s disease (PD), Dementia with Lewy bodies (DLB) and Multiple system atrophy (MSA). Although alpha-synuclein is a natively unfolded protein, fibrillization or conformational change(s) of alpha-synuclein is central to the pathogenesis of alpha-synucleinopathies. The amino-terminal region of alpha-synuclein consists of seven imperfect repeats, each 11 amino acids in length, with the consensus sequence KTKEGV. The repeats partially overlap with a hydrophobic region (amino acids 61-95). The carboxy-terminal region (amino acids 96-140) is negatively charged. These antibodies are powerful tools for biochemical and IHC analyses of neurodegenerative diseases and for evaluation of conformational changes of alpha-synuclein.

References:
1) Masami Masuda et al., Inhibition of a-synuclein fibril assembly by small molecules: Analysis using epitope-specific antibodies. FEBS Letters (2009) 583, 787-791. PMID 19183551
2) Motokuni Yonetani et al., Conversion of wild-type alpha-synuclein into mutant-type fibrils and its propagation in the presence of A30P mutant. Journal of Biological Chemistry (2009) 284, 7940-7950.
PMID 19164293

Application: ELISA

Clonality: Monoclonal

Host: Mouse

Purification: Ig-PG

Within the fields of molecular biology and pharmacology, a small molecule is a low molecular weight (< 900 daltons) organic compound that may regulate a biological process, with a size on the order of 1 nm. Most drugs are small molecules. Larger structures such as nucleic acids and proteins, and many polysaccharides are not small molecules, although their constituent monomers (ribo- or deoxyribonucleotides, amino acids, and monosaccharides, respectively) are often considered small molecules. Small molecules may be used as research tools to probe biological function as well as leads in the development of new therapeutic agents. Some can inhibit a specific function of a protein or disrupt protein–protein interactions.

Pharmacology usually restricts the term “small molecule” to molecules that bind specific biological macromolecules and act as an effector, altering the activity or function of the target. Small molecules can have a variety of biological functions or applications, serving as cell signaling molecules, drugs in medicine, pesticides in farming, and in many other roles. These compounds can be natural (such as secondary metabolites) or artificial (such as antiviral drugs); they may have a beneficial effect against a disease (such as drugs) or may be detrimental (such as teratogens and carcinogens). [from: Wikipedia contributors. (2019, April 6). Small molecule. In Wikipedia, The Free Encyclopedia. Retrieved 19:49, May 29, 2019, from https://en.wikipedia.org/w/index.php?title=Small_molecule&oldid=891243496]

Ginsenoside Re is a saponin isolated from Panax ginseng.

References:
1) Morinaga O. et al. (2006) Enzyme-linked immunosorbent assay for the determination of total ginsenosides in ginseng. Analytical Letters. 39:287-296.
2) Morinaga O, et al. (2006) Detection and quantification of ginsenoside Re in ginseng samples by a chromatographic immunostaining method using monoclonal antibody against ginsenoside Re. J Chromatogr B Analyt Technol Biomed Life Sci. 830(1):100-4. PMID: 16310421

Application: WB, IHC, RIA

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Bovine, Sheep, Mouse, Rat

Inhibin is an endocrine hormone produced in the ovaries, the testes and the placenta. This hormone has several functions in the body, with inhibin levels in women being linked to the menstrual cycle and playing a role in fetal development. Another hormone, activin, has an action in the body opposite to that of inhibin. Levels of these two hormones tend to fluctuate in both men and women in response to a number of cues which can include changes in hormone levels triggered by natural biological processes, environmental pressure, and other factors.

Application: IP, ELISA

Clonality: Monoclonal

Host: Rat

Purification: Ig-PG

Reactivity: Human

Squamous cell carcinoma antigen (SCCA) is a member of the ovalbumin family of serine proteinase inhibitors. The protein was isolated from a metastatic cervical squamous cell carcinoma by Kato and Torigoe (1977). SCCA is detected in the superficial and intermediate layers of normal squamous epithelium, whereas the mRNA is detected in the basal and sub-basal levels. The clinical import of SCCA has been as a circulating tumor marker for squamous cell carcinoma, especially those of the cervix, head and neck, lung, and esophagus. Many clinical studies of cervical squamous cell carcinoma show that the percentage of patients with elevated circulating levels of SCCA increases from approximately 12% at stage 0 to more than 90% at stage IV. Levels fall after tumor resection and rise in approximately 90% of the patients with recurrent disease. Similar trends occur in the other types of squamous cell carcinoma, with a maximum sensitivity of approximately 60% for lung, 50% for esophageal, and 55% for head and neck tumors. The neutral form of SCCA (SCCA1, or SERPINB3) is detected in the cytoplasm of normal and some malignant squamous cells, whereas the acidic form (SCCA2, or SERPINB4) is expressed primarily in malignant cells and is the major form found in the plasma of cancer patients. Thus, the appearance of the acidic fraction of SCCA is correlated with more aggressive tumors (summary by Schneider et al., 1995). Gene expression microarray profiling analysis has identified squamous cell cancer antigen (SCCA) as an IL-13 inflammation-induced gene in tracheal epithelial cells and keratinocytes.   SCCA expression is increased in asthmatic bronchiale and atopic dermatitis skin. Two isoforms of SCCA are known: SCCA1 and SCCA2. Anti-SCCA1/2 antibody is a rat monoclonal antibody which obtained from the immunization with purified, E. coli-derived, recombinant human SCCA1. This antibody can be used for the detection of human SCCA1 and SCCA2 by immunoprecipitation and ELISA.

Application: WB, IHC, IP

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Human, Mouse

Component of the RPD3C(L) histone deacetylase complex (HDAC). Responsible for the deacetylation of lysine residues on the N-terminal tails of core histones (H2A, H2B, H3 and H4). Histone deacetylation is a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. ASH1 is necessary to repress HO in daughter cells to block mating-type switching through its binding to HO promoter 5′-YTGAT-3′ sites. It is also involved in pseudohyphal growth.

Application: IP, IHC(p), WB, ELISA, IHC(f)

Clonality: Monoclonal

Host: Mouse

Purification: Ig-PG

Reactivity: Rat

Neurocan is a nervous tissue-unique, secretory proteoglycan that carries predominantly chondroitin sulfate side chains. Its expression gradually decreases with nervous tissue development. In the immature brain, neurocan exists in a full-length form with a 240 kDa-core glycoprotein, whereas in the mature brain it exists as proteolytic fragments of the NH2-terminal half (neurocan-N) with a 130 kDa-core glycopeptide and the COOH-terminal half (neurocan-C) with a 150 kDa-core glycopeptide. Neurocan is implicated in neural network formation and is a susceptibility factor for bipolar disorder. It is upregulated in central nervous system lesion sites and is a major component of glial scars. This antibody effectively recognizes the COOH-terminal half of rat neurocan core glycoprotein as well as the full length neurocan core glycoprotein.

Application: IHC(f), WB, IHC(p), IF

Clonality: Monoclonal

Host: Mouse

Purification: Ascities

Reactivity: Drosophila

Ca2+/calmodulin-dependent protein kinase II (CaM kinase II or CaMKII) is a serine/threonine-specific protein kinase that is regulated by the Ca2+/calmodulin complex. CaMKII is involved in many signaling cascades and is thought to be an important mediator of learning and memory.[1] CaMKII is also necessary for Ca2+ homeostasis and reuptake in cardiomyocytes,[2] chloride transport in epithelia,[3] positive T-cell selection,[4] and CD8 T-cell activation.[5] Misregulation of CaMKII is linked to Alzheimer’s disease, Angelman syndrome, and heart arrhythmia.[6]

Application: ELISA, IF, WB, IHC

Clonality: Monoclonal

Host: Mouse

Purification: Ig-PG

Background
Advanced Glycation End Product (AGE) is a general term for structures generated in the late stage of non-enzymatic glycation reactions (Millard reactions) between reducing sugars and proteins. AGE accumulation is known to be significantly elevated in age-related diseases such as diabetes and arteriosclerosis.

Nε-(carboxyethyl) lysine (CEL) is generated from protein modification by methylglyoxal (MG). MG is enzymatically derived from the Embden-Meyerhof and polyol pathways, through the degradation of glyceraldehyde-3-phosphate (G3P) (Phillips and Thornalley, 1993). Mclellan et al. (McLellan et al., 1994) demonstrated that plasma MG concentration in insulin-dependent diabetic patients was 7-times higher than in healthy individuals. CEL accumulation increases with age in human lens proteins.

Source: Professor Nagai Ryuji, Tokai University Faculty of Agriculture Department of Biosciences Food Bioregulation Research Laboratory

Product description

Package Size	50 µg
Form	Liquid (0.1M NaPB, pH7.0, 20 mg/ml BSA, 0.1% Sodium Azide (NaN3 ) added)
Concentration	1 mg/mL
Purity	Affinity Purified
Host	Rabbit Polyclonal
Immunogen	Synthetic phosphopeptide corresponding to residues L(44)S(p)PFYLRPPSF(54)C of human alpha-B Crystallin
Specificity	Alpha-B crystallin p45S
Cross Reactivity	Bovine, Human, Mouse, Rat
Subclass	IgG
Storage	Store below -20°C. Avoid freeze-thaw cycles.

 

Application: WB, IHC, IP

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Human, Mouse

Component of the Set-2/Ash-2 histone methyltransferase (HMT) complex. Required for di- and trimethylation at Lys-4 of histone H3, a mark associated with epigenetic transcriptional activation. Implicated in the epigenetic inheritance of lifespan over several generations. Functions as a transcriptional regulator. Acts in the germline to limit soma longevity, probably by regulating a lipid metabolism pathway that signals from the germline to the intestine, thereby preventing accumulation of mono-unsaturated fatty acids.

Application: ELISA, IHC(p), WB, IHC(f)

Clonality: Monoclonal

Host: Mouse

Purification: Supernatant

Reactivity: Human

COMP – cartilage oligomeric matrix protein – is a prominent multidomain glycoprotein of cartilage, accounting for up to 1% of the wet weight of articular tissues and having an approximate Mr of 97 kDa. COMP may also be found in tendon, bone (i.e. osteoblasts), ligament, certain smooth muscles and synovium. In the ECM COMP is present in a pentameric, disulfide-bonded complex with a Mr of about 550 kDa. Although the function of COMP is not completely elucidated, it appears to mediate chondrocyte attachment via integrins and to stabilize the articular cartilage ECM via specific cation-dependent interactions with collagen types II and IX, aggrecan, fibronectin, and ECM protein 1. In addition, mutations in the human COMP gene have been linked to the development of pseudoachondroplasia and multiple epiphyseal dysplasia, which are autosomal-dominant forms of short-limb dwarfism. In chondrocytes of these patients, COMP remains frequently entrapped in intracellular vesicles. COMP is a substrate for a variety of ECM degrading enzymes, including MMP-1, MMP-13, MMP-19, MMP20 and ADAMTS-4, -7 and -12. Fragments of COMP have been detected in the diseased cartilage, synovial fluid, and serum of patients with knee injuries, post-traumatic and primary osteoarthritis and rheumatoid arthritis and have proposed to be diagnostic/prognostic of degenerative cartilage diseases.

Application: WB, IF, IP, ELISA, IHC(p)

Clonality: Polyclonal

Host: Rabbit

Purification: Purified – Affinity

Reactivity: Human, Mouse, Rat

Background
Neurodegenerative diseases such as Alzheimer’s disease and Parkinson’s disease have been increasing rapidly and have become a serious social problem. In recent years, new causative genes have been discovered for amyotrophic lateral sclerosis (ALS) and other intractable neurological diseases opening new avenues for research on pathogenesis. It has been suggested that aggregation and accumulation of specific proteins cause neurotoxicity and the formation of lesions, but the onset and progression mechanisms are still unclear. Neuropathological diagnostic and experimental model biomarkers are needed for drug construction, drug discovery, and therapeutic development.

Vitamin D-dependent 28 kDa calcium-binding protein (calbindin D 28k or CB) is a member of the calmodulin superfamily of calcium binding proteins discovered in 1966 by Wasserman and Taylor. The protein has a distinct distribution in the brain and sensory system and is abundant in specific neuronal cell types. Calbindin D-28k constitutes as much as 0.1-1.5 % of the total soluble protein in brain and it may be present at intracellular concentrations up to 1 mM. Several recent studies have shown that calbindin D can protect cells from degeneration and ischemic injury under extracellular stress. In particular, this is demonstrated in the brain of Alzheimer and quotes disease patients. Cells containing calbindin D have a considerably lower plaque and tangles burden than those lacking this 28 kDa protein.

Applications

Western Blotting (WB): 0.1 µg/ml
Immunofluorescence (IF) : 1 µg/ml
Immunoprecipitation (IP) : assay dependent
Enzyme-linked immunosorbent assay (ELISA) : assay dependent
Immunohistochemistry (Paraffin) (IHC (P)) : assay dependent 

Product description

Package Size	50 µg
Form	Liquid (0.1M NaPB, pH7.0, 20 mg/ml BSA, 0.1% Sodium Azide (NaN3) added)
Concentration	1mg/ml
Purity	Affinity Purified
Host	Rabbit Polyclonal
Immunogen	28 kDa calbindin-D protein purified from rat kidney
Specificity	Calbindin D-28k
Cross Reactivity	Bovine, Human, Mouse, Porcine, Rat
Subclass	IgG
Storage	Store below -20°C. Avoid freeze-thaw cycles.

 

Application: ELISA, ICC, IP, IHC(p), WB, IF

Clonality: Polyclonal

Host: Rabbit

Purification: Purified – Affinity

Reactivity: Human, Rat

Background
Neurodegenerative diseases such as Alzheimer’s disease and Parkinson’s disease have been increasing rapidly and have become a serious social problem. In recent years, new causative genes have been discovered for amyotrophic lateral sclerosis (ALS) and other intractable neurological diseases opening new avenues for research on pathogenesis. It has been suggested that aggregation and accumulation of specific proteins cause neurotoxicity and the formation of lesions, but the onset and progression mechanisms are still unclear. Neuropathological diagnostic and experimental model biomarkers are needed for drug construction, drug discovery, and therapeutic development.

Parvalbumin (PV) is a calcium binding protein expressed in specific muscle fibers and fast-firing neurons. PV consists of a single, unbranched chain of linked amino acids and belongs to a larger group of EF hand proteins. Studies have demonstrated that parvalbumin acts in the decay of calcium in the contraction/relaxation cycle of fast twitch muscles. This data has shown a positive correlation between the rate of relaxation and the concentration of parvalbumin. Parvalbumin is also expressed in a specific population of GABAergic interneurons which are thought to play a role in maintaining the balance between excitation and inhibition in the cortex as well as the hippocampus. In amyotrophic lateral sclerosis (ALS) patents, parvalbumin immunoreactivity is specifically absent from neuron populations lost early in ALS.

Antigen/Source	Purified parvalbumin from rat skeletalmuscle.
Host	Rabbit
Immunogen	Rat
Reacts with	Human/Rat
Isotype	IgG
Fraction	Affinity Purified
Applications	Western Blot/IHC paraffin embedding section/Enzyme Linked Immunosorbent Assay/Immuno Fluorescence/Immunocytochemistry (cell)/Immunoprecipitation
Shape	Liquid
Preservative	0.1% NaN3
Storage	-20C

References
Inaguma Y, Kurobe N, Shinohara H, Kato K. (1991) Sensitive immunoassay for rat parvalbumin: tissue distribution and developmental changes. Biochim Biophys Acta. 1075: 68-74.

Application: IP, WB, IF, FC

Clonality: Monoclonal

Host: Mouse

Purification: Ig-PG

Reactivity: Human

CD63 (also known as LAMP-3, Melanoma-associated antigen ME491, TSPAN30, MLA1 and OMA81H) is a cell surface glycoprotein which belongs to the tetraspanin superfamily. CD63 is known to complex with integrins. CD63 is expressed on activated platelets, monocytes and macrophages and is weakly expressed on granulocytes, T cells and B cells. Importantly, it is found on the surface of exosomes.

Exosomes are cell-derived vesicles bounded by a lipid bilayer membrane and exhibiting a diameter of 50 to 150 nm. They are secreted from cultured cells and are observed in body fluids such as saliva, blood, urine, amniotic fluid, malignant ascites. Recent studies indicate that exosomes contain various proteins and RNAs, suggesting a role in information transfer between cells.

This monoclonal antibody can be used to immunoprecipitate exosomes from serum and culture supernatants.

References:
1) Yoshioka Y et al., Nat Commun. 2014 Apr 7;5:3591. doi: 10.1038/ncomms4591.
2) N Nishida-Aoki et al., Mol Ther. 2017 Jan 4;25(1):181-191. doi: 10.1016/j.ymthe.2016.10.009.
3) Saito S et al., Sci Rep. 2018 Mar 5;8(1):3997. doi: 10.1038/s41598-018-22450-2.

Application: ChIP, ICC, IHC, WB, IP

Clonality: Monoclonal

Host: Mouse

Purification: IgG

Reactivity: Mouse, Rat, Human, Hamster, Monkey

Application: IP, IF, WB, IHC(f)

Clonality: Monoclonal

Host: Mouse

Purification: Supernatant

Reactivity: Human

Hemidesmosomes are adhesive structures between cells and the extracellular matrix. They play a role in anchoring intermediate fibers to the extracellular basement membrane. Structurally, hemidesmosomes occur in two forms: Type I and Type II. Type I hemidesmosomes develop in stratified epithelia such as the epidermis. Its main components include the intracellular linker proteins Plectin and BPAG1, the adhesion receptor integrin α6β4 and collagen type BP180/XVII. Type II hemidesmosomes occur in blood vessels, Schwann cells, and digestive tract epithelia as a simplified form of Type I hemidesmosomes, consisting only plectin and integrin α6β4. The hemidesmosomal adhesion receptor is normally associated with Laminin 5 in the basement membrane. Furthermore, Laminin 5 (of which Laminin gamma 2 is a subunit) is linked to collagen fibers in the dermis via type VII collagen. Genetic deletion of hemidesmosome-related proteins causes various forms of epidermolysis bullosa, highlighting their importance in promoting adhesion between the epidermis and the basement membrane.

Unlike most collagens, collagen XVII is a transmembrane protein. Collagen XVII is a structural component of hemidesmosomes, multiprotein complexes at the dermal-epidermal basement membrane zone that mediate adhesion of keratinocytes to the underlying membrane. Mutations in this gene are associated with both generalized atrophic benign and junctional epidermolysis bullosa.

References:
1) Yamauchi T., et al. J. Dermatol. Sci., 76:25-33 (2014).
2) Hirako Y., et al. Exp. Cell Res., 324:172-182 (2014).
3) Hirako Y., et al. J. Baiol. Chem., 273:9711-9717 (1998).

Application: IP, ELISA

Clonality: Monoclonal

Host: Rat

Purification: Ig-PG

Reactivity: Human

Squamous cell carcinoma antigen (SCCA) is a member of the ovalbumin family of serine proteinase inhibitors. The protein was isolated from a metastatic cervical squamous cell carcinoma by Kato and Torigoe (1977). SCCA is detected in the superficial and intermediate layers of normal squamous epithelium, whereas the mRNA is detected in the basal and sub-basal levels. The clinical import of SCCA has been as a circulating tumor marker for squamous cell carcinoma, especially those of the cervix, head and neck, lung, and esophagus. Many clinical studies of cervical squamous cell carcinoma show that the percentage of patients with elevated circulating levels of SCCA increases from approximately 12% at stage 0 to more than 90% at stage IV. Levels fall after tumor resection and rise in approximately 90% of the patients with recurrent disease. Similar trends occur in the other types of squamous cell carcinoma, with a maximum sensitivity of approximately 60% for lung, 50% for esophageal, and 55% for head and neck tumors. The neutral form of SCCA (SCCA1, or SERPINB3) is detected in the cytoplasm of normal and some malignant squamous cells, whereas the acidic form (SCCA2, or SERPINB4) is expressed primarily in malignant cells and is the major form found in the plasma of cancer patients. Thus, the appearance of the acidic fraction of SCCA is correlated with more aggressive tumors (summary by Schneider et al., 1995). Gene expression microarray profiling analysis has identified squamous cell cancer antigen (SCCA) as an IL-13 inflammation-induced gene in tracheal epithelial cells and keratinocytes. SCCA expression is increased in asthmatic bronchiale and atopic dermatitis skin. Two isoforms of SCCA are known: SCCA1 and SCCA2. Anti-SCCA2 antibody is a rat monoclonal antibody raised against purified E. coli-derived, recombinant human SCCA2. This antibody can be used for the detection of human SCCA2 by immunoprecipitation and ELISA with no cross-reaction to SCCA1.

Source: Professor Kenji Dehara, Professor of Molecular Life Science, Faculty of Medicine, Saga University.

References:
1) The usefulness of combined measurements of squamous cell carcinoma antigens 1 and 2 in diagnosing atopic dermatitis. Shoichiro Ohta, et al. 2012. Ann Clin Biochem. 49: 277-284.
2) Characterization of novel squamous cell carcinoma antigen-related molecules in mice. Y. Sakata, et al. 2004. Biochem Biophys Res Commun. 324(4):1340-1345.
3) The squamous cell carcinoma antigens as relevant biomarkers of atopic dermatitis. K. Mitsuishi, et al. 2005. Clin Exp Allergy 35:1327-1333.
4) Involvement of IL-32 in activation-induced cell death in T cells. Chiho Goda, et al. 2006. Int Immunol 18(2):233-240.

Application: IHC, WB

Clonality: Monoclonal

Host: Rat

Purification: IgG

Reactivity: Monkey, Mouse, Rat, Human

Prohibitin, also known as PHB, is a protein that in humans is encoded by the PHB gene.[5] The Phb gene has also been described in animals, fungi, plants, and unicellular eukaryotes. Prohibitins are divided in two classes, termed Type-I and Type-II prohibitins, based on their similarity to yeast PHB1 and PHB2, respectively. Each organism has at least one copy of each type of prohibitin gene.[6][7] Prohibitins are evolutionarily conserved genes that are ubiquitously expressed. The human prohibitin gene, located on the BRCA1 chromosome region 17q21, was originally thought to be a negative regulator of cell proliferation and a tumor suppressor. This anti-proliferative activity was later attributed to the 3′ UTR of the PHB gene, and not to the actual protein. Mutations in human PHB have been linked to sporadic breast cancer. However, over-expression of PHB has been associated with a reduction in the androgen receptor activity and a reduction in PSA gene expression resulting in a decrease of androgen-dependent growth of cancerous prostate cells.[8] Prohibitin is expressed as two transcripts with varying lengths of 3′ untranslated region. The longer transcript is present at higher levels in proliferating tissues and cells, suggesting that this longer 3′ untranslated region may function as a trans-acting regulatory RNA.[5] Prohibitins are assembled into a ring-like structure with 16–20 alternating Phb1 and Phb2 subunits in the inner mitochondrial membrane.[9] The precise molecular function of the PHB complex is not clear, but a role as chaperone for respiration chain proteins or as a general structuring scaffold required for optimal mitochondrial morphology and function are suspected. Recently, prohibitins have been demonstrated to be positive, rather than negative, regulators of cell proliferation in both plants and mice. Both human prohibitins have also been suggested to be localized in the nucleus and modulate transcriptional activity by interacting with various transcription factors, including nuclear receptors, either directly or indirectly. However, little evidence for nuclear targeting and transcription factor-binding of prohibitins has been found in other organisms (yeast, plants, C. elegans, etc.), indicating that this may be a specific function in mammalian cells.[10][11][12][13] [from: Wikipedia contributors. (2019, February 20). Prohibitin. In Wikipedia, The Free Encyclopedia. Retrieved 18:24, June 4, 2019, from https://en.wikipedia.org/w/index.php?title=Prohibitin&oldid=884240489]

Application: IP, WB

Clonality: Polyclonal

Host: Rabbit

Purification: Ammonium Sulfate

Reactivity: Plant, Arabidopsis, Pea

Because plants have a sessile lifestyle, they must adjust to numerous external stimuli and coordinate their growth and development accordingly. The plant hormones, a group of structurally unrelated small molecules, are central to the integration of diverse environmental cues with a plant’s genetic program. The ‘classical’ phytohormones, identified during the first half of the twentieth century, are auxin, abscisic acid, cytokinin, gibberellin and ethylene. More recently, several additional compounds have been recognized as hormones, including brassinosteroids, jasmonate, salicylic acid, nitric oxide and strigolactones. Plants also use several peptide hormones to regulate various growth responses, but this class of hormones is beyond our scope here. With the application of genetic approaches, mainly in Arabidopsis thaliana, many aspects of hormone biology have been elucidated. Most hormones are involved in many different processes throughout plant growth and development. This complexity is reflected by the contributions of hormone synthesis, transport and signaling pathways, as well as by the diversity of interactions among hormones to control growth responses.

Genetic screens resulted in the identification of many of the proteins involved in hormone signaling and the analysis of these proteins has contributed significantly to our current models of hormone action. One particularly exciting outcome is the recent identification of receptors for auxin, gibberellin, jasmonate and abscisic acid. Though far from complete, our improved understanding of hormone perception and signaling has allowed for comparisons between hormones. From these it is clear that some hormones (cytokinins, ethylene and the brassinosteroids) use well-characterized signaling mechanisms. On the other hand, the identification and characterization of the auxin and jasmonate receptors, as well as proteins in gibberellin signaling, have highlighted a novel mechanism for hormone perception in which the ubiquitin–proteasome pathway has a central role. [from: Santner A., Mark E., Recent advances and emerging trends in plant hormone signalling (2009) Nature 459: 1071-1078]

Abscisic acid (ABA), a type of plant hormone, is thought to be involved in the induction of dormancy, stomatal closure, and physiological functions such as flower falling and leaf falling. The biosynthesis of this substance is carried out by oxidation of abscisin aldehyde, and it is suggested that a specific aldehyde oxidase (AO) catalyzes the reaction. The CosmoBio Antibody Collection (CAC) has prepared three antibodies for detecting AO gene products cloned from Arabidopsis thaliana, and an antibody for detection of corn ascorbic acid peroxidase (APT).

In higher plants aldehyde oxidases (AO) appear to be homo- and heterodimeric assemblies of AO subunits with probably different physiological functions. AO-delta seems to be involved in the last step of abscisic acid biosynthesis, at least in leaves and seeds. In vitro, AO-delta oxidizes abscisic aldehyde to abscisic acid (ABA). In vitro, AO-delta also uses indole-3-aldehyde (IAld), benzaldehyde, 1-naphthaldehyde and cinnamaldehyde as substrate; the AAO2-AAO3 dimer also uses abscisic aldehyde as substrate.

Source: Professor Koichi Koshiba, Tokyo Metropolitan University Graduate School of Science and Technology Department of Life Science

References:
Seo, M., Koiwai, H., Akaba, S., Komano, T., Oritani, T., Kamiya, Y. and Koshiba, T. (2000) Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana. Plant J. 23:481-488.

Application: IF, IHC(p), WB

Clonality: Polyclonal

Host: Rabbit

Purification: Purified – Affinity

Reactivity: Bovine, Human, Mouse, Rat

Background

Neurodegenerative diseases such as Alzheimer’s disease and Parkinson’s disease have been increasing rapidly and have become a serious social problem. In recent years, new causative genes have been discovered for amyotrophic lateral sclerosis (ALS) and other intractable neurological diseases opening new avenues for research on pathogenesis. It has been suggested that aggregation and accumulation of specific proteins cause neurotoxicity and the formation of lesions, but the onset and progression mechanisms are still unclear. Neuropathological diagnostic and experimental model biomarkers are needed for drug construction, drug discovery, and therapeutic development.

Lens proteins consist almost entirely of crystallins (about 95%). Crystallins are also found in vertebrate skeletal muscle tissue. In the lens, their structural function is to assist in maintaining the proper refractive index of the lens. The mammalian lens contains 3 major classes of crystallins: alpha, beta, and gamma. Alpha-crystallin is the largest of the crystallins and is composed of 2 primary gene products, alpha-A and alpha-B. There are at least 5 different proteins comprising the beta-crystallins. The gamma-crystallins are monomeric, but there are at least 5 gamma crystallins identified in bovine and rat lens.
Alpha-Crystallin comprises 40% of total lens protein composition. In addition to maintaining proper refractive index, it also functions in a chaperone like manner by preventing the formation of aggregates possibly leading to cataract formation. It is believed that the phosphorylated states of the alpha-crystallin occur in response to cellular stress and may serve a structural control function and play a role in protein maintenance. Alpha-B crystallin has been linked to Alexander and quotes disease where it accumulates in brain cells of those afflicted.

Applications

Western Blotting (WB):0.5 µg/ml
Immunofluorescence (IF):5 µg/ml
Immunohistochemistry (Paraffin) (IHC (P)): 10 µg/ml

Product description

Package Size	50 µg
Form	Liquid (0.1M NaPB, pH7.0, 20 mg/ml BSA, 0.1% Sodium Azide (NaN3) added)
Concentration	1 mg/mL
Purity	Affinity Purified
Host	Rabbit Polyclonal
Immunogen	Synthetic phosphopeptide corresponding to residues F(14)FPFHS(p)PSRLFD(25) of human alpha-B Crystallin
Specificity	Alpha-B crystallin p59S
Cross Reactivity	Bovine, Human, Mouse, Rat
Subclass	IgG
Storage	Store below -20°C. Avoid freeze-thaw cycles.

References
1) Ito H, Okamoto K, Nakayama H, Isobe T, Kato K. (1997) Phosphorylation of B-crystallin in response to various types of stress. J Biol Chem. 272, 29934-29941.
2) Kato K, Ito H, Kamei K, Inaguma Y, Iwamoto I, Saga S. (1998) Phosphorylation of B-crystallin in mitotic cells and identification of enzymatic activities responsible for phosphorylation. J Biol Chem. 273, 28346-28354.
3) Ito H, Iida K, Kamei K, Iwamoto I, Inaguma Y, Kato K. (1999) B-crystallin in rat lens is phosphorylated at an early postnatal age. FEBS Lett. 446, 269-272.

Application: WB, IEM

Clonality: Monoclonal

Host: Mouse

Purification: Ig-PG

Reactivity: Plant, Fish, Yeast, Rat, Human, Frog

Regulating protein stability and turnover is a key task in the cell. Besides lysosomes, ubiquitin‐mediated proteasomal degradation comprises the major proteolytic pathway in eukaryotes. Proteins destined for degradation by the proteasome are conjugated by a ‘tag’, a ubiquitin chain to a lysine, through an extensively regulated enzymatic cascade. The ubiquitylated proteins are subsequently targeted for degradation by the 26S proteasome, the major proteolytic machinery for ubiquitylated proteins in the cell. Ubiquitylation can be considered as another covalent post‐translational modification and signal, comparable to acetylation, glycosylation, methylation, and phosphorylation. However, ubiquitylation has multiple roles in addition to targeting proteins for degradation. Depending on the number of ubiquitin moieties and the linkages made, ubiquitin also plays an important role in DNA repair, protein sorting and virus budding. Unregulated degradation of proteins, or abnormally stable proteins, interfere with several regulatory pathways, and the ubiquitin‐proteasome pathway is affected in a number of diseases, such as neurodegenerative diseases, cellular atrophies and malignancies. Therefore, dissecting the ubiquitin‐proteasome pathway and identifying proteins involved in conjunction with the signals required for specific degradation of certain substrates, would help in developing novel therapeutic approaches to treat diseases where the ubiquitin‐proteasome pathway is impaired. [from: Roos‐Mattjus P. and Sistonen L. The ubiquitin‐proteasome pathway (2009) Annals of Medicine 36(4): 285-295]

The 26S proteasome is an essential component of the ubiquitin-proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins. It is composed of a 20S proteasome catalytic core and regulatory particles at either end. The subunits of the 20S proteasome are classified into two families, α and β. In eukaryotes, the 20S proteasome contains seven α-type subunits and seven β-type subunits. The fourteen subunits are arranged in four rings of seven and form an α7β7β7α7 structure. This antibody recognizes α2 subunit of the 20S proteasome from all organisms tested, yeast to human and is suitable for immuno-electron microscopy.

References:
1) Tokumoto, T., Tokumoto, M., Seto, K., Horiguchi, R., Nagahama, Y., Yamada, S., Ishikawa, K., Lohka, M. J. 1999. Disappearance of a novel protein component of the 26S proteasome during Xenopus oocyte maturation. Exp Cell Res 247, 313-319.. PubMed: 10066358
2) Wakata, Y., Tokumoto, M., Horiguchi, R., Ishikawa, K., Nagahama, Y., Tokumoto, T. 2004. Identification of alpha-type subunits of the Xenopus 20S proteasome and analysis of their changes during the meiotic cell cycle. BMC Biochem 5, 18. PubMed: 15603592
3) Tokumoto, M., Horiguchi, R., Nagahama, Y., Ishikawa, K., Tokumoto, T. 2000. Two proteins, a goldfish 20S proteasome subunit and the protein interacting with 26S proteasome, change in the meiotic cell cycle. Eur J Biochem 267, 97-103. PubMed: 10601855

Application: IP, ChIP, ELISA, IHC, WB

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Drosophila

FACT (Facilitates Chromatin Transcription) is a protein complex involved in chromatin remodeling and comprises two subunits, SSRP1 and SPT16. A recent Drosophila study suggested that FACT forms a complex with a DNA binding protein, GAGA factor, to regulate sequence-specific changes in chromatin structure. SSRP1 and SPT16 have come to be noted as important new factors linking FACT and GAGA factors.

dSPT16 is the Drosophila ortholog of SPT16. Studies hve revealed that dSPT16 facilitates various chromatin transactions such as transcriptional regulation, DNA replication and histone replacement. This antibody against dSPT16 is a powerful tool for Western blots (Ref.1), immunostaining (Ref.2), immunoprecipitation and chromatin immunopreciptation (Ref.1,2,3).

Source: Dr. Susumu Hirose, National Institute of Genetics

References:
1) Shimojima, T. et al. , (2003) Genes & Dev . 17, 1605-1616.
2) Saunders, A. et al. , (2003) Science , 301, 1094-1096.
3) Nakayama, T. et al. , (2007) Genes & Dev . 21, 552-561.

Application: FC, ELISA, IHC

Clonality: Polyclonal

Host: Rat

Purification: Serum

Reactivity: Rat, Human

Neurodegenerative diseases such as Alzheimer’s disease and Parkinson’s disease have been increasing rapidly and have become a serious social problem. In recent years, new causative genes have been discovered for amyotrophic lateral sclerosis (ALS) and other intractable neurological diseases opening new avenues for research on pathogenesis. It has been suggested that aggregation and accumulation of specific proteins cause neurotoxicity and the formation of lesions, but the onset and progression mechanisms are still unclear. Neuropathological diagnostic and experimental model biomarkers are needed for drug construction, drug discovery, and therapeutic development.

ITIH4 is secreted into the blood and is cleaved by plasma kallikrein into two protein fragments. The expression of this protein is localized to the liver, and peptide fragments of ITIH4 are detected in the serum of patients with liver cancer and cirrhosis. Thus, ITIH4 is a new biomarker for liver disease. Furthermore, experiments using model mice with amyotrophic lateral sclerosis (ALS) have shown that ITIH4 elevation promotes progression of pathological conditions. On the other hand, ITIH4 has many sites that undergo post-translational modification such as glycosylation, and its application to cell staining and flow cytometry by antibodies using peptides and recombinant proteins as antigens has been considered extremely difficult. These problems have been solved by the nanotaxi method, and we present two rat polyclonal antibodies suitable for detection of human ITIH4.

Application: ELISA, IHC, IF

Clonality: Polyclonal

Host: Mouse

Purification: Serum

Reactivity: Mouse

WDR45L is a ubiquitously expressed WD40 repeat protein upregulated in a variety of tumor tissues including ovarian and uterine cancers. WDR45L, also known as WIPI-3, comprises seven 40 amino acid (WD40) repeats. WD40 repeats are found in many eukaryotic proteins that coordinate multi-protein complex assemblies. WD40 proteins are implicated in multiple functions, including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly. This protein regulates cell cycle transcription and signal transduction, and it is believed to be involved in cell death by apoptosis and autophagy. In recent years, it has also been used as a marker for neurodegenerative diseases associated with cell death.

Application: FC, WB

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Human

Human recombinant IL-32 does not exhibit similarities with known cytokine families, yet several properties are typical of a pro-inflammatory cytokine. It was discovered accidentally while studying the genes induced by IL-18 and was found to stimulate the production of various chemokines, pro-inflammatory cytokines including IL-1β, IL-6, IL-8, TNF-α and macrophage inflammatory protein-2 (MIP-2). Inflammation or infection with various pathogens including Mycobacterium tuberculosis, Epstein-Barr virus (EBV), human immunodeficiency virus (HIV) and influenza A virus have been reported to induce the expression of IL-32. The IL-32 gene is located on human chromosome 16 p13.3, which is organized into eight exons with six splice variants of the gene; these variants have been described as IL-32α, IL-32β, IL-32γ, IL-32δ, IL-32ε and IL-32ζ, of which, IL-32α is the most abundant transcript. Anti-tumor activity of NK cells is provoked by IL-12 and IL-18, both of which induce IL-32 production that stimulates TNF-α synthesis enhancing NK apoptotic activity. IL-32 was found in cytosol as well as in the nucleus. Park et al. reported that IL-32 enhances the anti-tumor activity specifically for NK-92 cells upon introduction of the death receptor and the activation of caspase-3 pathway in cancer cells. IL-32 has been reported to play a key role in the pathogenesis of various disorders, including infectious autoimmune and inflammatory diseases. Anti-IL-32 polyclonal antibody obtained from rabbit immunization with purified E. coli-derived recombinant human IL-32. This antibody can be used for the detection of IL-32 by immunoblotting and flow cytometry.

References:
Goda, C et al., Int. Immunol. 18:233-240, 2006

Application: WB

Clonality: Monoclonal

Host: Mouse

Purification: IgG

Background
Detection of intracellular AID plasmid (pAID1.1-N Vector, pAID1.1-C Vector or Luc-AID NLS plasmid) expression is very critical for scientists who integrate them into cells. Anti-AID protein tag antibody (IAA17) provides an excellent means for monitoring gene expression and protein localization in living cells. Monoclonal anti-AID tag (IAA17) antibody can detect AID tag (IAA17) in immunoblot experiments.

Application

This antibody reacts with IAA17 on Western blotting. This antibody also detects AID tag conjugated with protein expressed in mammalian cells and Yeast cells on Western blotting.

WB : 1 : 500 – 1 : 2,000
Other applications have not been tested

Feature and Advantages

The mouse was immunized with recombinant AID tag (IAA17) protein.
This antibody was purified from mouse using Purified IgG

This antibody solution contains PBS, and 0.1% sodium azide as preservative.
*Azide may react with copper or lead in plumbing system to form explosive metal azides. Please always flush plenty of water when disposing materials containing azide to drain.

References
Nature Methods (2009) 6:917-923.

Application: FC

Clonality: Monoclonal

Host: Rat

Purification: IgG

Reactivity: Human

The interleukin-13 receptor is a type I cytokine receptor, binding Interleukin-13. It consists of two subunits, encoded by IL13RA1 and IL4R, respectively. These two genes encode the proteins IL-13Rα1 and IL-4Rα. These form a dimer with IL-13 binding to the IL-13Rα1 chain and IL-4Rα stabilises this interaction. This IL-13 receptor can also instigate IL-4 signalling. In both cases this occurs via activation of the Janus kinase (JAK)/Signal Transducer and Activator of Transcription (STAT) pathway, resulting in phosphorylation of STAT6. Phosphorylated STAT6 dimerises and acts as a transcription factor activating many genes, such as eotaxin.

Application: ELISA, WB

Clonality: Polyclonal

Host: Rabbit

Purification: Purified – Affinity

Reactivity: Human, Rat

TGF-β is produced as a pro-protein in which the 25 kD active TGF-β is trapped by an N-terminal pro-peptide called Latency Associated Protein (LAP). Upon receipt of certain stimuli a conformational change is induced in a latent complex to release the active TGF-β from the complex. The resultant TGF-β binds to cognate signaling receptors and exerts various physiological and pathological activities. This reaction is called TGF-β activation reaction, which is known to be induced by binding of the latent complex to cell adhesion proteins such as thrombospondin and integrins, and/or by being cleaved by the action of proteases such as serine proteases, cysteine proteases, and MMPs in an organ and context-depending manner. The RIKEN Center for Biomedical Science and Research Center for Liver Cancer Prevention and Research Unit focused on the involvement of the serine protease plasmin and plasma kallikrein in the release and activation of TGF-β and its involvement in liver diseases. They showed that plasmin and plasma kallikrein cleave, respectively, at 56Lys-57Leu and 58Arg-59Leu within the LAP portion of the latent TGF-β1 molecule. The anti-TGF-β1 LAP-degradates (LAP-D) antibodies are useful to investigate the molecular mechanism of TGF-β activation and its related diseases including liver fibrosis/cirrhosis and liver degeneration.

Source: Professor Koichi, National Institute of Advanced Industrial Science and Technology RIKEN Biomedical Science Research Center Liver Cancer Prevention Research Unit

References:
Kojima, S. et al., “Detection and prevention of hepatic fibrosis targetingTGF-β activation reaction” Hepatology
46(4): 712A (2007).

Application: WB, IHC, ELISA, IP

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Human

Metastasis suppressor protein in malignant melanomas and in some breast cancers. May regulate events downstream of cell-matrix adhesion, perhaps involving cytoskeletal reorganization. Generates a C-terminally amidated peptide, Metastin, which functions as the endogenous ligand of the G-protein coupled receptor GPR54. Activation of the receptor inhibits cell proliferation and cell migration, key characteristics of tumor metastasis.

Application: IHC, WB, ELISA

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Human, Mouse

Neurodegenerative diseases such as Alzheimer’s disease and Parkinson’s disease have been increasing rapidly and have become a serious social problem. In recent years, new causative genes have been discovered for amyotrophic lateral sclerosis (ALS) and other intractable neurological diseases opening new avenues for research on pathogenesis. It has been suggested that aggregation and accumulation of specific proteins cause neurotoxicity and the formation of lesions, but the onset and progression mechanisms are still unclear. Neuropathological diagnostic and experimental model biomarkers are needed for drug construction, drug discovery, and therapeutic development.

Alpha-Synuclein, a 140-amino acid protein abundantly expressed in presynaptic terminals, is a component of intraneuronal or glial inclusions observed in cases of Parkinson’s disease (PD), Dementia with Lewy bodies (DLB) and Multiple system atrophy (MSA). Although alpha-synuclein is a natively unfolded protein, fibrillization or conformational change(s) of alpha-synuclein is central to the pathogenesis of alpha-synucleinopathies. The amino-terminal region of alpha-synuclein consists of seven imperfect repeats, each 11 amino acids in length, with the consensus sequence KTKEGV. The repeats partially overlap with a hydrophobic region (amino acids 61-95). The carboxy-terminal region (amino acids 96-140) is negatively charged. These antibodies are powerful tools for biochemical and IHC analyses of neurodegenerative diseases and for evaluation of conformational changes of alpha-synuclein.

References:
1) Masami Masuda et al., Inhibition of a-synuclein fibril assembly by small molecules: Analysis using epitope-specific antibodies. FEBS Letters (2009) 583, 787-791. PMID 19183551
2) Motokuni Yonetani et al., Conversion of wild-type alpha-synuclein into mutant-type fibrils and its propagation in the presence of A30P mutant. Journal of Biological Chemistry (2009) 284, 7940-7950. PMID 19164293

Application: FC

Clonality: Monoclonal

Host: Rat

Purification: Ig-PG

Reactivity: Mouse

CD44 is a single-pass type I transmembrane protein and functions as a cellular adhesion molecule for hyaluronic acid, a major component of the extracellular matrix. It exists in numerous isoforms that are generated through alternative splicing of CD44 precursor mRNA. Whereas the standard isoform of CD44 (CD44s) is expressed predominantly in hematopoietic cells and normal epithelial cell subsets, CD44v (variant) isoforms, which contain additional insertions in the membrane-proximal extracellular region, are highly expressed in epithelial-type carcinomas. Moreover, CD44 is reported to be a cell surface marker for cancer stem cells (CSCs) derived from solid tumors including breast, prostate, colon, head and neck and pancreatic cancer. Expression of CD44, especially variant isoforms (CD44 v8-10), contributes to reactive oxygen species (ROS) defense through upregulation of the synthesis of reduced glutathione (GSH), the primary intracellular antioxidant. CD44 v8-10 interacts with and stabilizes xCT, a subunit of the cystine-glutamate transporter xc(-), and thereby promotes cystine uptake for GSH synthesis. The ability to avoid the consequences of exposure to high levels of ROS is required for cancer cell survival and propagation in vivo. CSCs (whose defense against ROS is enhanced by CD44v8-10) are thus thought to drive tumor growth, chemoresistance and metastasis. Clone RM1 (a monoclonal antibody specific for mouse CD44 v10-e16) can be used in flow cytometry, and importantly, for the enrichment of CSCs using FACS. RM1 can be applied towards understanding a variety of molecular mechanisms for cancer stem cells using in vitro cell-based assays such as “in vitro sphere formation” and “in vivo lung metastasis” assays.

References:
1) Nagano O., et al., Oncogene. 2013 Jan 21., 1-8.
2) Ishimoto T., et al., Cancer Cell. 2011 Mar 8;19(3):387-400.
3) Yae T., et al., Nat Commun. 2012 Jun 6;3:883.
4) Tsugawa H., et al., Cell Host Microbe. 2012 Dec 13;12(6):764-77.
5) Tanabe KK., et al., Lancet. 1993 Mar 20;341(8847):725-6.

Application: WB, IP, IHC

Clonality: Monoclonal

Host: Mouse

Purification: Purified – Affinity

Reactivity: Bovine, Mouse, Rat, Human

Lect1 encodes a glycosylated transmembrane protein that is cleaved to form a mature, secreted protein. The N-terminus of the precursor protein shares characteristics with other surfactant proteins and is sometimes called chondrosurfactant protein, although no biological activity has yet been defined for it. The C-terminus of the precursor protein contains a 25 kDa mature protein called leukocyte cell-derived chemotaxin-1 or chondromodulin-1. The mature protein promotes chondrocyte growth and inhibits angiogenesis. This gene is expressed in the avascular zone of prehypertrophic cartilage, and its expression decreases during chondrocyte hypertrophy and vascular invasion. The mature protein likely plays a role in endochondral bone development by permitting cartilaginous anlagen to be vascularized and replaced by bone. It may also be involved in the broad control of tissue vascularization during development. Alternative splicing results in multiple transcript variants encoding different isoforms.[7] [from: Wikipedia contributors. (2017, October 27). LECT1. In Wikipedia, The Free Encyclopedia. Retrieved 17:42, June 3, 2019, from https://en.wikipedia.org/w/index.php?title=LECT1&oldid=807301938]

Application: ELISA

Clonality: Monoclonal

Host: Mouse

Purification: Ammonium Sulfate

Within the fields of molecular biology and pharmacology, a small molecule is a low molecular weight (< 900 daltons) organic compound that may regulate a biological process, with a size on the order of 1 nm. Most drugs are small molecules. Larger structures such as nucleic acids and proteins, and many polysaccharides are not small molecules, although their constituent monomers (ribo- or deoxyribonucleotides, amino acids, and monosaccharides, respectively) are often considered small molecules. Small molecules may be used as research tools to probe biological function as well as leads in the development of new therapeutic agents. Some can inhibit a specific function of a protein or disrupt protein–protein interactions.

Pharmacology usually restricts the term “small molecule” to molecules that bind specific biological macromolecules and act as an effector, altering the activity or function of the target. Small molecules can have a variety of biological functions or applications, serving as cell signaling molecules, drugs in medicine, pesticides in farming, and in many other roles. These compounds can be natural (such as secondary metabolites) or artificial (such as antiviral drugs); they may have a beneficial effect against a disease (such as drugs) or may be detrimental (such as teratogens and carcinogens). [from: Wikipedia contributors. (2019, April 6). Small molecule. In Wikipedia, The Free Encyclopedia. Retrieved 19:49, May 29, 2019, from https://en.wikipedia.org/w/index.php?title=Small_molecule&oldid=891243496]

5-Fluorouracil (5-FU) is a pyrimidine analogue and inhibits an enzyme called thymidylate synthetase, which results in inhibition of DNA replication. Thus, 5-FU is used as a drug in the treatment of cancers including colorectal cancer, pancreatic cancer and skin cancer.

Application: IHC, Neutralization, RIA

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Avian, Chicken

Gonadotropin Releasing Hormone (GnRH), also know as Luteinizing-hormone-releasing-hormone (LHRH) and luliberin, is a tropic peptide hormone responsible for the release of follicle-stimulating hormone (FSH) and Luteinizing Hormone (LH) from the anterior pituitary. GnRH is synthesized and released from neurons within the hypothalamus. The peptide belongs to gonadotropin-releasing hormone family.

Application: IP, ELISA, IHC(p), WB

Clonality: Monoclonal

Host: Mouse

Purification: Supernatant

Reactivity: Human

Aggrecan is the major proteoglycan in articular cartilage (synthesized by mature chondrocytes) and in perineuronal nets of the CNS. While its precise function around CNS neurons remains obscure, in articular cartilage it contributes to creating the hydrated gel structure of the ECM via its interaction with hyaluronan, link protein, CMPs, COMP and collagen type IX. Deletion of the aggrecan gene causes early disturbances in chondrogenesis and brain defects. Aggrecan is a multimodular molecule whose core protein is composed of three globular domains denoted G1, G2, and G3, a large extended region spanning the portion of the molecule between the globular domains G1 and G2 and containing the majority of the GAG attachment sites and a second GAG-bearing inter-globular domain (IGD) occurs between G2 and G3. The GAG attachment domain between G1 and G2 contains mainly chondroitin sulphate chains (up to 40) and some keratan sulfate chains. The inter-globular G2-G3 domain exclusively bears keratan sulphate chains. The corresponding core protein region of sclera and brain aggrecans do not seem to contain keratan sulphates. The G1 amino-terminal domain of the aggrecan core protein has the same structural motif as link protein and is responsible for the binding of the proteoglycan to hyaluronan and link protein. The G2 globular domain is homologous to the tandem repeats of G1 and of link protein and is crucial for the synthesis and cellular secretion of aggrecan. The G3 globular domain makes up the carboxyl terminus of the core protein and is similarly responsible for post-translational processing of the proteoglycan and its secretion, as well as for its molecular interactions with other cartilage ECM components. Fully glycosylated/glycanated aggrecan of articular cartilage has an average size of 2,400-2,500 kDa, but its Mr may vary with age and the conditions of the cartilage tissue. The non-glycosylated/non-glycanated core protein has an approximate Mr of 240 kDa.

References:
Virgintino D, et all., (2009) Aggrecan isoforms of perineuronal nets identify subsets of parvalbumin and calbindin neurons differentially distributed in cortical layers II-VI of human adult cortex. J. Cell. Mol. Medicine 13, 3151-3173.I161:I164.

Application: ELISA

Clonality: Monoclonal

Host: Mouse

Purification: Ig-PG

Within the fields of molecular biology and pharmacology, a small molecule is a low molecular weight (< 900 daltons) organic compound that may regulate a biological process, with a size on the order of 1 nm. Most drugs are small molecules. Larger structures such as nucleic acids and proteins, and many polysaccharides are not small molecules, although their constituent monomers (ribo- or deoxyribonucleotides, amino acids, and monosaccharides, respectively) are often considered small molecules. Small molecules may be used as research tools to probe biological function as well as leads in the development of new therapeutic agents. Some can inhibit a specific function of a protein or disrupt protein–protein interactions.

Pharmacology usually restricts the term “small molecule” to molecules that bind specific biological macromolecules and act as an effector, altering the activity or function of the target. Small molecules can have a variety of biological functions or applications, serving as cell signaling molecules, drugs in medicine, pesticides in farming, and in many other roles. These compounds can be natural (such as secondary metabolites) or artificial (such as antiviral drugs); they may have a beneficial effect against a disease (such as drugs) or may be detrimental (such as teratogens and carcinogens). [from: Wikipedia contributors. (2019, April 6). Small molecule. In Wikipedia, The Free Encyclopedia. Retrieved 19:49, May 29, 2019, from https://en.wikipedia.org/w/index.php?title=Small_molecule&oldid=891243496]

Salvinorin is a psychoactive terpene isolated from Salvia divinorum.

References:
Madan Kumar Paudel, Osamu Shirota, Kaori Sasaki-Tabata, Hiroyuki Tanaka, Setsuko Sekita, and Satoshi Morimoto. (2013) Development of an Enzyme Immunoassay Using a Monoclonal Antibody against the Psychoactive Diterpenoid Salvinorin A. Journal of Natural Products. 76(9):1654-1660. DOI: 10.1021/np400358n.

Application: FC

Clonality: Polyclonal

Host: Mouse

Purification: Serum

Reactivity: Mouse

Translocator protein (TSPO) is an 18 kDa protein mainly found on the outer mitochondrial membrane. It was first described as peripheral benzodiazepine receptor (PBR), a secondary binding site for diazepam, but subsequent research has found the receptor to be expressed throughout the body and brain.[5] In humans, the translocator protein is encoded by the TSPO gene.[6][7] It belongs to family of tryptophan-rich sensory proteins. Regarding intramitochondrial cholesterol transport, TSPO has been proposed to interact with StAR (steroidogenic acute regulatory protein) to transport cholesterol into mitochondria, though evidence is mixed.[8] In animals, TSPO (PBR) is a mitochondrial protein usually located in the outer mitochondrial membrane and characterized by its ability to bind a variety of benzodiazepine-like drugs, as well as to dicarboxylic tetrapyrrole intermediates of the haem biosynthetic pathway. TSPO has many proposed functions depending on the tissue.[9] The most studied of these include roles in the immune response, steroid synthesis and apoptosis. [from: Wikipedia contributors. (2019, April 29). Translocator protein. In Wikipedia, The Free Encyclopedia. Retrieved 18:37, June 4, 2019, from https://en.wikipedia.org/w/index.php?title=Translocator_protein&oldid=894679824]

Application: EIA, RIA

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Human, Mouse, Rat, Bovine, Chicken

Testosterone is the primary male sex hormone and an anabolic steroid. In male humans, testosterone plays a key role in the development of male reproductive tissues such as testes and prostate, as well as promoting secondary sexual characteristics such as increased muscle and bone mass, and the growth of body hair.[3] In addition, testosterone is involved in health and well-being,[4] and the prevention of osteoporosis.[5] Insufficient levels of testosterone in men may lead to abnormalities including frailty and bone loss. Testosterone is a steroid from the androstane class containing a keto and hydroxyl groups at the three and seventeen positions respectively. It is biosynthesized in several steps from cholesterol and is converted in the liver to inactive metabolites.[6] It exerts its action through binding to and activation of the androgen receptor.[6] In humans and most other vertebrates, testosterone is secreted primarily by the testicles of males and, to a lesser extent, the ovaries of females. On average, in adult males, levels of testosterone are about 7 to 8 times as great as in adult females.[7] As the metabolism of testosterone in males is more pronounced, the daily production is about 20 times greater in men.[8][9] Females are also more sensitive to the hormone.[10] In addition to its role as a natural hormone, testosterone is used as a medication, for instance in the treatment of low testosterone levels in men, hormone replacement therapy in transgender men, and breast cancer in women.[11] Since testosterone levels decrease as men age, testosterone is sometimes used in older men to counteract this deficiency. It is also used illicitly to enhance physique and performance, for instance in athletes. In general, androgens such as testosterone promote protein synthesis and thus growth of tissues with androgen receptors.[12] Testosterone can be described as having virializing and anabolic effects (though these categorical descriptions are somewhat arbitrary, as there is a great deal of mutual overlap between them).[13]

• Anabolic effects include growth of muscle mass and strength, increased bone density and strength, and stimulation of linear growth and bone maturation.
• Androgenic effects include maturation of the sex organs, particularly the penis and the formation of the scrotum in the fetus, and after birth (usually at puberty) a deepening of the voice, growth of facial hair (such as the beard) and axillary (underarm) hair. Many of these fall into the category of male secondary sex characteristics.

Testosterone effects can also be classified by the age of usual occurrence. For postnatal effects in both males and females, these are mostly dependent on the levels and duration of circulating free testosterone. [from: Wikipedia contributors. (2019, June 2). Testosterone. In Wikipedia, The Free Encyclopedia. Retrieved 20:39, June 3, 2019, from https://en.wikipedia.org/w/index.php?title=Testosterone&oldid=899958411]

Application: IHC, WB

Clonality: Polyclonal

Host: Rabbit

Purification: Ig-PA

Reactivity: Mouse, Rat

EVC is a gene associated with Ellis-van Creveld syndrome. It overlaps with the CRMP1 gene.[1] EVC is one of two genes (the other being EVC2) that upon mutation give rise to EvC (Ellis-van Creveld) syndrome in humans and is found to act as a positive mediator for three hedgehog (Hh) signaling molecules.[2] Mice with an inactivation of the EVC gene (EVC -/-) were found to exhibit similar physical characteristics as humans, such as shortened limbs and dental impairments.[2] In a study of 65 individuals affected with EvC, mutations in the EVC gene were found in 20 of them, and primarily attributed to a frameshift resulting in a nonsense codon.[3] More mild physical characteristics not completely associated with EvC syndrome, such as those without the expected oral deformities can also be attributed to EVC gene mutations.[4] [from: Wikipedia contributors. (2019, May 3). EVC (gene). In Wikipedia, The Free Encyclopedia. Retrieved 19:37, June 3, 2019, from https://en.wikipedia.org/w/index.php?title=EVC_(gene)&oldid=895336273]

Application: WB

Clonality: Monoclonal

Host: Mouse

Purification: Ig-PA

Reactivity: Dog

Neural cell adhesion molecule (NCAM), also called CD56, is a homophilic binding glycoprotein expressed on the surface of neurons, glia and skeletal muscle. Although CD56 is often considered a marker of neural lineage commitment due to its discovery site, CD56 expression is also found in, among others, the hematopoietic system. Here, the expression of CD56 is most stringently associated with, but certainly not limited to, natural killer cells. CD56 has been detected on other lymphoid cells, including gamma delta (γδ) Τ cells and activated CD8+ T cells, as well as on dendritic cells.[5] NCAM has been implicated as having a role in cell–cell adhesion,[6] neurite outgrowth, synaptic plasticity, and learning and memory. During hematopoiesis, CD56 is the prototypic marker of NK cells, also present on subset of CD4+ T cells and CD8+ T cells. [from: Wikipedia contributors. (2019, May 24). Neural cell adhesion molecule. In Wikipedia, The Free Encyclopedia. Retrieved 16:41, June 4, 2019, from https://en.wikipedia.org/w/index.php?title=Neural_cell_adhesion_molecule&oldid=898602503]

References:
1) Koike A., Uematsu Y., Bonkobara M., Yamaguchi T., Washizu T., Arai T. (2007) 144th Annual Meeting of Japanese Society of Veterinary Science, I-39.
2) Uematsu Y, Yamaguchi T, Koike A, Yagihara H, Hasegawa D, Matsuki N, Ono K, Washizu T, Arai T, Bonkobara M. (2008) Generation of Monoclonal Antibody against Canine Neural-Cell Adhesion Molecule. Journal of Veterinary Medical Science. 70(8):845-847.

Application: WB, IHC, IP

Clonality: Monoclonal

Host: Mouse

Purification: Purified – Affinity

Reactivity: Bovine, Mouse, Rat, Human

Lect1 encodes a glycosylated transmembrane protein that is cleaved to form a mature, secreted protein. The N-terminus of the precursor protein shares characteristics with other surfactant proteins and is sometimes called chondrosurfactant protein, although no biological activity has yet been defined for it. The C-terminus of the precursor protein contains a 25 kDa mature protein called leukocyte cell-derived chemotaxin-1 or chondromodulin-1. The mature protein promotes chondrocyte growth and inhibits angiogenesis. This gene is expressed in the avascular zone of prehypertrophic cartilage, and its expression decreases during chondrocyte hypertrophy and vascular invasion. The mature protein likely plays a role in endochondral bone development by permitting cartilaginous anlagen to be vascularized and replaced by bone. It may also be involved in the broad control of tissue vascularization during development. Alternative splicing results in multiple transcript variants encoding different isoforms.[7] [from: Wikipedia contributors. (2017, October 27). LECT1. In Wikipedia, The Free Encyclopedia. Retrieved 17:42, June 3, 2019, from https://en.wikipedia.org/w/index.php?title=LECT1&oldid=807301938]

Application: WB, IHC

Clonality: Monoclonal

Host: Mouse

Purification: Supernatant

Reactivity: Human

The RhoGAP family encompasses a unique member named SDP35 (also referred to as DEPDC1, DEP8, FLJ20354 or DEPDC1-V2) and pairing with a homologue named XTP1 (also referred to as DEPDC1B, BRCC3 or FLJ11252).The structural-functional properties of SDP35 are still largely unknown, but its structural uniqueness resides in the presence of a domain showing homology with Dishwelled, i.e. the DEP domain (Dishwelled/Pleckstrin-like domain). The presence of this domain suggests that SDP35 might engage in more complex molecular interactions than those of other members of the family. Another peculiar feature of SDP35 is represented by its atypical GAP domain, which lacks the orthodox “Arg finger” catalytic motif essential for exerting canonical GAP function. Whereas most RhoGAP family members are either ubiquitously expressed throughout the body or are concentrated in discrete tissue/organs, SDP35 is remarkably poorly represented in most human tissues (also supported by evidence provided by the Comparative Cancer Genome Project database). SDP35 has been reported to be up-regulated in bladder cancer and numerous cancer cell types.

Application: IF, IHC(f)

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Mouse, Rat

transport protein (variously referred to as a transmembrane pump, transporter, escort protein, acid transport protein, cation transport protein, or anion transport protein) is a protein that serves the function of moving other materials within an organism. Transport proteins are vital to the growth and life of all living things. There are several different kinds of transport proteins. Carrier proteins are proteins involved in the movement of ions, small molecules, or macromolecules, such as another protein, across a biological membrane.[1] Carrier proteins are integral membrane proteins; that is, they exist within and span the membrane across which they transport substances. The proteins may assist in the movement of substances by facilitated diffusion (i.e., passive transport) or active transport. These mechanisms of movement are known as carrier-mediated transport.[2] Each carrier protein is designed to recognize only one substance or one group of very similar substances. Research has correlated defects in specific carrier proteins with specific diseases.[3] A membrane transport protein (or simply transporter) is a membrane protein[4] that acts as such a carrier. [from: Wikipedia contributors. (2019, May 9). Transport protein. In Wikipedia, The Free Encyclopedia. Retrieved 18:43, June 6, 2019, from https://en.wikipedia.org/w/index.php?title=Transport_protein&oldid=896329420]

Glucose transporter 2 (GLUT2) also known as solute carrier family 2 (facilitated glucose transporter), member 2 (SLC2A2) is a transmembrane carrier protein that enables protein facilitated glucose movement across cell membranes. It is the principal transporter for transfer of glucose between liver and blood [5] Unlike GLUT4, it does not rely on insulin for facilitated diffusion. GLUT2 has high capacity for glucose but low affinity (high Km, ca. 15-20 mM) and thus functions as part of the “glucose sensor” in the pancreatic β-cells of rodents, though in human β-cells the role of GLUT2 seems to be a minor one.[10] It is a very efficient carrier for glucose.[11][12] GLUT2 also carries glucosamine.[13] When the glucose concentration in the lumen of the small intestine goes above 30 mM, such as occurs in the fed-state, GLUT2 is up-regulated at the brush border membrane, enhancing the capacity of glucose transport. Basolateral GLUT2 in enterocytes also aids in the transport of fructose into the bloodstream through glucose-dependent cotransport.

References:
1) Thorens B, Cheng ZQ, Brown D, Lodish HF. (1990) Liver glucose transporter: a basolateral protein in hepatocytes and intestine and kidney cells. J Am Physiol. 259(2 Pt 1):C279-85.

Prolonged exposure to solar UV radiation may result in harmful acute and chronic effects to the skin (including skin cancers), eye, and immune system. These harmful effects appear to be closely related to UV-induced DNA damage. Indeed, UV-induced DNA damage plays significant roles in cell-cycle arrest, activation of DNA repair, cell killing, mutation, and neoplastic transformation. The major types of DNA damage induced by solar UV radiation are cyclobutane pyrimidine dimers (CPDs), (6–4) photoproducts (6-4PPs), and Dewar valence isomers of 6-4PPs (Dewar photoproducts; DewarPPs) formed between adjacent pyrimidine nucleotides on the same DNA strand. Approximately 70-80% of UV-induced DNA damage is CPDs and the remaining is 6-4PPs and Dewar isomers of 6-4PPs. DewarPPs are produced by the photoisomerization of 6-4PPs by UV radiation around 325 nm. In normal human cells these types of DNA lesions are repaired by nucleotide excision repair (NER).

To better study molecular events surrounding UV-induced DNA damage and repair, Mori et al. previously developed and characterized monoclonal antibody (mAb) specific for CPDs and mAb specific for 6-4PPs (1) while Matsunaga et al. developed and characterized mAb specific for DewarPPs (2). Three of these antibodies (CPDs: clone TDM-2; 6-4PPs: clone 64M-2; DewarPPs: clone DEM-1) continue to be cited frequently in the literature, often for use in ELISA.

This High Sensitivity Cyclobutane Pyrimidine Dimers (CPDs) ELISA Kit is the only commercially available ELISA utilizing anti-CPDs clone TDM-2 and has been optimized for high sensitivity detection of CPDs in DNA purified from cultured cells or from skin epidermis. This ELISA detects CPDs from dipyrimidines in all DNA sequence contexts (i.e., TT, TC, CT and CC). Thus, the availability and convenience of this ELISA Kit will contribute to further understanding molecular mechanisms involved in cellular responses to UV radiation and DNA damage with applications across many research fields including cancer research, photobiology, dermatology, ophthalmology, immunology, and cosmetics science.

References:

1) Yamamoto, A., et al., DNA Repair, 6, 649-657 (2007).

2) Matsumoto, M., et al., J. Cell Sci., 120, 1104-1112 (2007).

3) Yasuda, G., et al., Mol. Cell. Biol., 27, 6606-6614 (2007).

4) Sugasawa, K., et al., Cell 121, 387-400 (2005).

5) Nishiwaki, Y., et al., J. Invest. Dermatol. 122, 526-532 (2004).

6) Imoto, K., et al., J. Invest. Dermatol. 119, 1177-7782 (2002).

7) Wakasugi, M., et al., J. Biol. Chem., 277, 1637-1640 (2002).

8) Kobayashi, N., et al., Pigment Cell Res. 14, 94-102 (2001).

9) Katsumi, S., et al., J. Invest. Dermatol. 117, 1156-1161 (2001).

10) Otoshi, E., et al., Cancer Res. 60, 1729-1735 (2000).

11) Nakagawa, A., et al., J. Invest. Dermatol. 110, 143-148 (1998).

12) Kobayashi, N., et al., J. Invest. Dermatol. 110, 806-810 (1998).

13) Komatsu, Y., et al., Nucleic Acids Res. 25, 3889-3894 (1997).

14) Nakane, H., et al., Nature 377, 165-168 (1995).

15) Todo, T., et al., Nature 361, 371-374 (1993).

16) Kobayashi, N., et al., J. Invest. Dermatol. 101, 685-689 (1993).

17) Potten, C.S., et al., Int. J. Radiat. Biol. 63, 313-324 (1993).

18) Matsunaga, T., et al., Photochem. Photobiol. 54, 403-410 (1991).

19) Mori, T., et al., Photochem. Photobiol. 54, 225-232 (1991).

More than 200 papers using TDM-2 and 64M-2 antibodies have been published so far.

Application: WB

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Aequorea victoria

Anti EGFP antibody is a rabbit polyclonal antibody obtained from rabbit immunization with purified E. coli-derived recombinant EGFP. This antibody has been tested and confirmed for use in immunoblotting against enhanced GFP.

Application: IEM, IHC(f), WB, IF, ICC

Clonality: Monoclonal

Host: Mouse

Purification: Ig-PG

Reactivity: Plant, Fish, Yeast, Rat, Human, Frog

Regulating protein stability and turnover is a key task in the cell. Besides lysosomes, ubiquitin‐mediated proteasomal degradation comprises the major proteolytic pathway in eukaryotes. Proteins destined for degradation by the proteasome are conjugated by a ‘tag’, a ubiquitin chain to a lysine, through an extensively regulated enzymatic cascade. The ubiquitylated proteins are subsequently targeted for degradation by the 26S proteasome, the major proteolytic machinery for ubiquitylated proteins in the cell. Ubiquitylation can be considered as another covalent post‐translational modification and signal, comparable to acetylation, glycosylation, methylation, and phosphorylation. However, ubiquitylation has multiple roles in addition to targeting proteins for degradation. Depending on the number of ubiquitin moieties and the linkages made, ubiquitin also plays an important role in DNA repair, protein sorting and virus budding. Unregulated degradation of proteins, or abnormally stable proteins, interfere with several regulatory pathways, and the ubiquitin‐proteasome pathway is affected in a number of diseases, such as neurodegenerative diseases, cellular atrophies and malignancies. Therefore, dissecting the ubiquitin‐proteasome pathway and identifying proteins involved in conjunction with the signals required for specific degradation of certain substrates, would help in developing novel therapeutic approaches to treat diseases where the ubiquitin‐proteasome pathway is impaired. [from: Roos‐Mattjus P. and Sistonen L. The ubiquitin‐proteasome pathway (2009) Annals of Medicine 36(4): 285-295]

The 26S proteasome is an essential component of the ubiquitin-proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins. It is composed of a 20S proteasome catalytic core and regulatory particles at either end. The subunits of the 20S proteasome are classified into two families, α and β. In eukaryotes, the 20S proteasome contains seven α-type subunits and seven β-type subunits. The fourteen subunits are arranged in four rings of seven and form an α7β7β7α7 structure. This antibody recognizes multiple subunits of the 20S proteasome from all organisms tested from yeast to human and is suitable for immunoelectron microscopy.

References:
1) Haraguchi, C. M., Mabuchi, T., Hirata, S., Shoda, T., Tokumoto, T., Hoshi, K., Yokota, S. 2007. Possible function of caudal nuclear pocket: degradation of nucleoproteins by ubiquitin-proteasome system in rat spermatids and human sperm. J Histochem Cytochem 55, 585-595. PubMed: 17312012
2) Ohsaki, Y., Cheng, J., Fujita, A., Tokumoto, T., Fujimoto, T. 2006. Cytoplasmic lipid droplets are sites of convergence of proteasomal and autophagic degradation of apolipoprotein B. Mol Biol Cell 17, 2674-2683. PubMed: 16597703
3) Tokumoto, M., Horiguchi, R., Nagahama, Y., Ishikawa, K., Tokumoto, T. 2000. Two proteins, a goldfish 20S proteasome subunit and the protein interacting with 26S proteasome, change in the meiotic cell cycle. Eur J Biochem 267, 97-103. PubMed: 10601855

Application: FC

Clonality: Monoclonal

Conjugation: Tide Fluor™5

Host: Mouse

Purification: Ig-PG

Reactivity: Human

CD9 is a cell surface glycoprotein which belongs to the tetraspanin superfamily. CD9 is known to complex with integrins and other transmembrane 4 superfamily proteins. It can modulate cell adhesion and migration and also trigger platelet activation and aggregation. Importantly, it is found on the surface of exosomes.

Exosomes are cell-derived vesicles bounded by a lipid bilayer membrane and exhibiting a diameter of 50 to 150 nm. They are secreted from cultured cells and are observed in body fluids such as saliva, blood, urine, amniotic fluid, malignant ascites. Recent studies indicate that exosomes contain various proteins and RNAs, suggesting a role in information transfer between cells.

This monoclonal antibody can be used to immunoprecipitate exosomes from serum and culture supernatants.

References:
1) Shigeyasu Tsuda et al., Scientific Reports volume 7, Article number: 12989 (2017)
2) N Nishida-Aoki et al., Mol Ther. 2017 Jan 4;25(1):181-191. doi: 10.1016/j.ymthe.2016.10.009.
3) Matsuzaki K et al., Oncotarget. 2017 Apr 11; 8(15): 24668–24678. doi: 10.18632/oncotarget.14969
4) Kazutoshi Fujita et al., Sci Rep. 2017; 7: 42961. doi: 10.1038/srep42961
5) Yoshioka Y et al., Nat Commun. 2014 Apr 7;5:3591. doi: 10.1038/ncomms4591.
6) Saito S et al., Sci Rep. 2018 Mar 5;8(1):3997. doi: 10.1038/s41598-018-22450-2.
7) Yagi Y et al., Neurosci Lett. 2017 Jan 1;636:48-57. doi: 10.1016/j.neulet.2016.10.042. Epub 2016 Oct 22.
8) Ueda K et al., Sci Rep. 2014 Aug 29;4:6232. doi: 10.1038/srep06232.

Application: ICC, WB, IF

Clonality: Monoclonal

Host: Rat

Purification: IgG

Reactivity: Mouse

Transcription factors (TFs) directly interpret the genome, performing the first step in decoding the DNA sequence. Many function as ‘‘master regulators’’ and ‘‘selector genes’’, exerting control over processes that specify cell types and developmental patterning (Lee and Young, 2013) and controlling specific pathways such as immune responses (Singh et al., 2014). In the laboratory, TFs can drive cell differentiation (Fong and Tapscott, 2013) and even de-differentiation and trans-differentiation (Takahashi and Yamanaka, 2016). Mutations in TFs and TF-binding sites underlie many human diseases. Their protein sequences, regulatory regions, and physiological roles are often deeply conserved among metazoans (Bejerano et al., 2004; Carroll, 2008), suggesting that global gene regulatory ‘‘networks’’ may be similarly conserved. And yet, there is high turnover in individual regulatory sequences (Weirauch and Hughes, 2010), and over longer timescales, TFs duplicate and diverge. The same TF can regulate different genes in different cell types (e.g., ESR1 in breast and endometrial cell lines [Gertz et al., 2012]), indicating that regulatory networks are dynamic even within the same organism. Determining how TFs are assembled in different ways to recognize binding sites and control transcription is daunting yet paramount to under-standing their physiological roles, decoding specific functional properties of genomes, and mapping how highly specific expression programs are orchestrated in complex organisms. [from: Lambert SA, Jolma A, Campitelli LF, Das PK, Yin Y. (2018) The Human Transcription Factors. Cell. 172:650-665.]

Oct4/Pou5f1 is a member of POU transcription factor family, which possess POU domain. This transcription factor forms a trimeric complex with SOX2 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206. Oct4/Pou5f1 is critical for early embryogenesis and for embryonic stem cell pluripotency.

References:
1) Sterneckert, J. et al. (2012) Oct4 and More: The Reprogramming Expressway. Stem Cells. 30(1):15-21.